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P53618 (COPB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Coatomer subunit beta
Alternative name(s):
Beta-coat protein
Short name=Beta-COP
Gene names
Name:COPB1
Synonyms:COPB
ORF Names:MSTP026
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length953 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte surface triglyceride lipase (PNPLA2) with the lipid droplet to mediate lipolysis By similarity. Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1. Promotes degradation of Nef cellular targets CD4 and MHC class I antigens by facilitating their trafficking to degradative compartments. Ref.10 Ref.12 Ref.15 Ref.17

Subunit structure

Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Interacts (via C-terminus) with HIV-1 Nef; the interaction is direct. Interacts with SCYL1. Interacts with COPG1. Interacts (via trunk domain) with ARF1 (via switch I region); the interaction is direct. Interacts with KCNK2/TREK (via N-terminus); this interaction increases the channel-mediated whole cell currents and promotes plasma membrane expression of KCNK2/TREK. Interacts with anthrax lethal factor (LF); this interaction may facilitate endosomal vesicle membrane translocation of LF and its release from the lumen of endosomal vesicles to external milieu. Interacts with CAPN8 and PRKCE By similarity. Interacts with ARF1 (myristoylated); this interaction is required for binding of COPB1 to Golgi membranes By similarity. Interacts with STX17 By similarity. Ref.6 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.16

Subcellular location

Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicleCOPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane. Endoplasmic reticulum-Golgi intermediate compartment. Note: The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Proteolytic cleavage by CAPN8 triggers translocation from Golgi to cytoplasm By similarity. Found in perinuclear vesicular-tubular clusters (VTCs) and in the Golgi region where associated with vesicles, buds and rims of the Golgi stack By similarity. Occasionally present at the trans-side of Golgi, but mainly present at the cis-Golgi side in transitional areas (TA), on so-called peripheral elements (PE) consisting of tubules and vesicles located between the cup-shaped transitional elements (TE) of the rough endoplasmic reticulum (RER) and the cis-most Golgi cisternae By similarity. Present in cytoplasm, not associated with visible coats or membranes, with a minor fraction present on small clusters of tubules and vesicles By similarity. Some association with high-density and low-density microsomes and mitochondria/nuclei fraction By similarity. Very little found in plasma membrane fraction By similarity. Ref.7 Ref.8 Ref.9 Ref.10 Ref.16 Ref.17

Post-translational modification

Proteolytically cleaved between Ser-528 and Ser-529 by CAPN8 By similarity.

Miscellaneous

Brefeldin A induces dissociation from the Golgi of the beta-COP and presumably the other coatomer subunits.

Sequence similarities

Contains 6 HEAT repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SUN2Q9UH992EBI-359063,EBI-1044964

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 953952Coatomer subunit beta
PRO_0000193833

Regions

Repeat96 – 13136HEAT 1
Repeat132 – 16837HEAT 2
Repeat240 – 27637HEAT 3
Repeat277 – 31438HEAT 4
Repeat316 – 35338HEAT 5
Repeat396 – 43338HEAT 6

Amino acid modifications

Modified residue21N-acetylthreonine Ref.14
Modified residue4941N6-acetyllysine By similarity

Experimental info

Sequence conflict8251D → E in AAD41240. Ref.1
Sequence conflict8251D → E in CAA57622. Ref.6
Sequence conflict8471F → L in AAD41240. Ref.1
Sequence conflict8471F → L in CAA57622. Ref.6
Sequence conflict9111I → S in AAD41240. Ref.1
Sequence conflict9111I → S in CAA57622. Ref.6
Sequence conflict9151I → L in AAD41240. Ref.1
Sequence conflict9151I → L in CAA57622. Ref.6
Sequence conflict9251G → V in AAD41240. Ref.1
Sequence conflict9251G → V in CAA57622. Ref.6
Sequence conflict9501K → E in AAD41240. Ref.1
Sequence conflict9501K → E in CAA57622. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P53618 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: BE916C1C5A599D79

FASTA953107,142
        10         20         30         40         50         60 
MTAAENVCYT LINVPMDSEP PSEISLKNDL EKGDVKSKTE ALKKVIIMIL NGEKLPGLLM 

        70         80         90        100        110        120 
TIIRFVLPLQ DHTIKKLLLV FWEIVPKTTP DGRLLHEMIL VCDAYRKDLQ HPNEFIRGST 

       130        140        150        160        170        180 
LRFLCKLKEA ELLEPLMPAI RACLEHRHSY VRRNAVLAIY TIYRNFEHLI PDAPELIHDF 

       190        200        210        220        230        240 
LVNEKDASCK RNAFMMLIHA DQDRALDYLS TCIDQVQTFG DILQLVIVEL IYKVCHANPS 

       250        260        270        280        290        300 
ERARFIRCIY NLLQSSSPAV KYEAAGTLVT LSSAPTAIKA AAQCYIDLII KESDNNVKLI 

       310        320        330        340        350        360 
VLDRLIELKE HPAHERVLQD LVMDILRVLS TPDLEVRKKT LQLALDLVSS RNVEELVIVL 

       370        380        390        400        410        420 
KKEVIKTNNV SEHEDTDKYR QLLVRTLHSC SVRFPDMAAN VIPVLMEFLS DNNEAAAADV 

       430        440        450        460        470        480 
LEFVREAIQR FDNLRMLIVE KMLEVFHAIK SVKIYRGALW ILGEYCSTKE DIQSVMTEIR 

       490        500        510        520        530        540 
RSLGEIPIVE SEIKKEAGEL KPEEEITVGP VQKLVTEMGT YATQSALSSS RPTKKEEDRP 

       550        560        570        580        590        600 
PLRGFLLDGD FFVAASLATT LTKIALRYVA LVQEKKKQNS FVAEAMLLMA TILHLGKSSL 

       610        620        630        640        650        660 
PKKPITDDDV DRISLCLKVL SECSPLMNDI FNKECRQSLS HMLSAKLEEE KLSQKKESEK 

       670        680        690        700        710        720 
RNVTVQPDDP ISFMQLTAKN EMNCKEDQFQ LSLLAAMGNT QRKEAADPLA SKLNKVTQLT 

       730        740        750        760        770        780 
GFSDPVYAEA YVHVNQYDIV LDVLVVNQTS DTLQNCTLEL ATLGDLKLVE KPSPLTLAPH 

       790        800        810        820        830        840 
DFANIKANVK VASTENGIIF GNIVYDVSGA ASDRNCVVLS DIHIDIMDYI QPATCTDAEF 

       850        860        870        880        890        900 
RQMWAEFEWE NKVTVNTNMV DLNDYLQHIL KSTNMKCLTP EKALSGYCGF MAANLYARSI 

       910        920        930        940        950 
FGEDALANVS IEKPIHQGPD AAVTGHIRIR AKSQGMALSL GDKINLSQKK TSI 

« Hide

References

« Hide 'large scale' references
[1]"Human beta-cop homolog gene, complete CDS."
Zhang J., Liu T., Fu G., Li W., Ye M., Zhou J., Wu J., Shen Y., Yu M., Chen S., Mao M., Chen Z.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Xu Y.Y., Sun L.Z., Wu Q.Y., Liu Y.Q., Liu B., Zhao B., Wang X.Y., Song L., Ye J., Sheng H., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Sun Y.H., Jiang Y.X., Zhao X.W., Liu S. expand/collapse author list , Liu L.S., Ding J.F., Gao R.L., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Aorta.
[3]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Amygdala.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[6]"Physical interaction of the HIV-1 Nef protein with beta-COP, a component of non-clathrin-coated vesicles essential for membrane traffic."
Benichou S., Bomsel M., Bodeus M., Durand H., Doute M., Letourneur F., Camonis J., Benarous R.
J. Biol. Chem. 269:30073-30076(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 651-953, INTERACTION WITH HIV-1 NEF.
Tissue: Lymphoid tissue.
[7]"The oculocerebrorenal syndrome gene product is a 105-kD protein localized to the Golgi complex."
Olivos-Glander I.M., Janne P.A., Nussbaum R.L.
Am. J. Hum. Genet. 57:817-823(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"Identification and characterization of novel isoforms of COP I subunits."
Futatsumori M., Kasai K., Takatsu H., Shin H.-W., Nakayama K.
J. Biochem. 128:793-801(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COPG1, SUBUNIT, SUBCELLULAR LOCATION.
[9]"Multiple and stepwise interactions between coatomer and ADP-ribosylation factor-1 (Arf1)-GTP."
Sun Z., Anderl F., Frohlich K., Zhao L., Hanke S., Brugger B., Wieland F., Bethune J.
Traffic 8:582-593(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARF1, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[10]"Depletion of beta-COP reveals a role for COP-I in compartmentalization of secretory compartments and in biosynthetic transport of caveolin-1."
Styers M.L., O'Connor A.K., Grabski R., Cormet-Boyaka E., Sztul E.
Am. J. Physiol. 294:C1485-C1498(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"Scyl1, mutated in a recessive form of spinocerebellar neurodegeneration, regulates COPI-mediated retrograde traffic."
Burman J.L., Bourbonniere L., Philie J., Stroh T., Dejgaard S.Y., Presley J.F., McPherson P.S.
J. Biol. Chem. 283:22774-22786(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCYL1.
[12]"HIV-1 Nef targets MHC-I and CD4 for degradation via a final common beta-COP-dependent pathway in T cells."
Schaefer M.R., Wonderlich E.R., Roeth J.F., Leonard J.A., Collins K.L.
PLoS Pathog. 4:E1000131-E1000131(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HIV-1 NEF.
[13]"COPI coatomer complex proteins facilitate the translocation of anthrax lethal factor across vesicular membranes in vitro."
Tamayo A.G., Bharti A., Trujillo C., Harrison R., Murphy J.R.
Proc. Natl. Acad. Sci. U.S.A. 105:5254-5259(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ANTHRAX LETHAL FACTOR.
[14]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[15]"Early endosomes and endosomal coatomer are required for autophagy."
Razi M., Chan E.Y., Tooze S.A.
J. Cell Biol. 185:305-321(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Enhancement of TREK1 channel surface expression by protein-protein interaction with beta-COP."
Kim E., Hwang E.M., Yarishkin O., Yoo J.C., Kim D., Park N., Cho M., Lee Y.S., Sun C.H., Yi G.S., Yoo J., Kang D., Han J., Hong S.G., Park J.Y.
Biochem. Biophys. Res. Commun. 395:244-250(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KCNK2, SUBCELLULAR LOCATION.
[17]"Quantitative proteomics analysis of cell cycle-regulated Golgi disassembly and reassembly."
Chen X., Simon E.S., Xiang Y., Kachman M., Andrews P.C., Wang Y.
J. Biol. Chem. 285:7197-7207(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF084457 mRNA. Translation: AAD41240.1.
AF111807 mRNA. Translation: AAL39009.1.
AL136593 mRNA. Translation: CAB66528.1.
CH471064 Genomic DNA. Translation: EAW68481.1.
CH471064 Genomic DNA. Translation: EAW68482.1.
CH471064 Genomic DNA. Translation: EAW68483.1.
CH471064 Genomic DNA. Translation: EAW68484.1.
CH471064 Genomic DNA. Translation: EAW68485.1.
BC037280 mRNA. Translation: AAH37280.1.
X82103 mRNA. Translation: CAA57622.1.
PIRA55136.
T46913.
RefSeqNP_001137533.1. NM_001144061.1.
NP_001137534.1. NM_001144062.1.
NP_057535.1. NM_016451.4.
XP_005252851.1. XM_005252794.1.
UniGeneHs.339278.

3D structure databases

ProteinModelPortalP53618.
SMRP53618. Positions 119-164, 400-430.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107710. 56 interactions.
DIPDIP-265N.
IntActP53618. 32 interactions.
MINTMINT-1151935.
STRING9606.ENSP00000249923.

PTM databases

PhosphoSiteP53618.

Polymorphism databases

DMDM116241311.

Proteomic databases

PaxDbP53618.
PeptideAtlasP53618.
PRIDEP53618.

Protocols and materials databases

DNASU1315.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000249923; ENSP00000249923; ENSG00000129083.
ENST00000439561; ENSP00000397873; ENSG00000129083.
GeneID1315.
KEGGhsa:1315.
UCSCuc001mlg.2. human.

Organism-specific databases

CTD1315.
GeneCardsGC11M014436.
H-InvDBHIX0009466.
HGNCHGNC:2231. COPB1.
HPACAB012338.
HPA040166.
HPA043954.
MIM600959. gene.
neXtProtNX_P53618.
PharmGKBPA26747.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5096.
HOGENOMHOG000207417.
HOVERGENHBG005380.
InParanoidP53618.
KOK17301.
OMAVRTLHTC.
OrthoDBEOG7ZWD12.
TreeFamTF105737.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpressP53618.
BgeeP53618.
CleanExHS_COPB1.
GenevestigatorP53618.

Family and domain databases

Gene3D1.25.10.10. 3 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR011710. Coatomer_bsu_C.
IPR016460. COPB1.
[Graphical view]
PANTHERPTHR10635. PTHR10635. 1 hit.
PfamPF01602. Adaptin_N. 1 hit.
PF07718. Coatamer_beta_C. 1 hit.
[Graphical view]
PIRSFPIRSF005727. Coatomer_beta_subunit. 1 hit.
SUPFAMSSF48371. SSF48371. 2 hits.
ProtoNetSearch...

Other

ChiTaRSCOPB1. human.
GeneWikiCOPB1.
GenomeRNAi1315.
NextBio5379.
PROP53618.
SOURCESearch...

Entry information

Entry nameCOPB_HUMAN
AccessionPrimary (citable) accession number: P53618
Secondary accession number(s): D3DQX0 expand/collapse secondary AC list , Q6GTT7, Q9NTK2, Q9UNW7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 17, 2006
Last modified: March 19, 2014
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM